Entry: P30761 Genes: rpoC ML1890 Length: 1316 aa

DNA-directed RNA polymerase subunit beta' (RNAP subunit beta')

RPOC_MYCLE • Mycobacterium leprae (strain TN)
Navigate Overview Model Scores RCSB 1D Mol* Pockets B-Cell Epitopes Function and interactions Ontology and localisation Sequence features and PTMs Evidence and cross-references

Summary

Download FASTA UniProt: P30761 ML Locus: ML1890
Entry P30761
Reviewed reviewed
Entry Name RPOC_MYCLE
Gene Names rpoC ML1890
ML locus tag ML1890
Organism Mycobacterium leprae (strain TN)
Length 1316 aa
Mass 146896 Da
Annotation 3.0
Annotation Summary

Evidence and cross-references

PubMed ID 8446028; 11234002
DOI ID 10.1111/j.1365-2958.1993.tb01112.x; 10.1038/35059006
STRING 272631.gene:17575738;
KEGG mle:ML1890;
eggNOG COG0086;
OrthoDB 9815296at2;
InterPro IPR045867;IPR012754;IPR000722;IPR006592;IPR007080;IPR007066;IPR042102;IPR007083;IPR007081;IPR044893;IPR038120;

Oligomer Models

Best Boltz2 oligomer and local AlphaFold‑3 homooligomer structure models matched to ML1890, with the same model switching, Mol*, Nightingale, pLDDT, PAE, and download functionality as monomers.
Count: 1
Assembly Method Template / Source Overall Rank Download
heterooligomer Boltz2 — — Download Model

Ligands

Curated ligands imported from the selected oligomer template/YAML rows. The displayed ligand code is the original template CCD code; predicted-model placeholders such as LIG1/LIG2 are not shown. Click a ligand code to focus the ligand in Mol*.
Ligands: 0
Ligand Code Ligand Name PubChem ID
No curated ligand rows were found for this oligomer in the database.

Monomer Models

Monomer structure models for ML1890, retaining all existing model selection, Mol*, Nightingale, pLDDT, PAE, and download functionality.
Count: 4
Assembly Method Model Overall Rank Download
Monomer Boltz2 0 0.799797 Download Model
Monomer AlphaFold‑3 1 0.917600 Download Model
Monomer Boltz 0 0.804238 Download Model
Monomer CHAI 0 0.177352 Download Model

Sequence & Feature Viewer

Residue-level feature tracks for the loaded model — pLDDT confidence colouring, mapped annotations, and interactive PAE selection ranges. Drag a region on the heatmap to highlight it here and in Mol*.
RCSB 1D
Sequence viewer will initialise once a structure model is loaded.
Mol* — ML1890

Mol* Structure Viewer

Local mmCIF model display for ML1890 with Mol* controls hidden.
Default: heterooligomer • Boltz2
Preparing heterooligomer • Boltz2 model 0 for ML1890…
Residue focus: none
Heterooligomer ML IDs / chain selection

PAE Map Panel

Predicted aligned error heatmap for the currently loaded model, when pairwise confidence data are available in the local mmCIF.
PAE • Waiting for Model
PAE Heatmap
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Scored residue
Aligned residue
Hover over the heatmap to inspect residue-pair PAE values.
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B-cell Epitope Propensity

Per-residue conformational B-cell epitope predictions from DiscoTope-3.0.
Epitope · Loading
Low
Epitope
Residue number Residue type DiscoTope-3.0 score Focus
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Annotation Summary

Function and interactions

EC number 2.7.7.6
Catalytic activity CATALYTIC ACTIVITY: Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate; Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
Binding site BINDING 60; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 62; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 75; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 78; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 535; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 537; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 539; /ligand="Mg(2+)"; /ligand_id="ChEBI:CHEBI:18420"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 891; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 968; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 975; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"; BINDING 978; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
Cofactor COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01322}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_01322}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
Subunit structure SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription. {ECO:0000255|HAMAP-Rule:MF_01322}.
Annotation Summary

Ontology and localisation

Gene Ontology (biological process) DNA-templated transcription [GO:0006351]
Gene Ontology (cellular component) cytosol [GO:0005829]; DNA-directed RNA polymerase complex [GO:0000428]
Gene Ontology (GO) cytosol [GO:0005829]; DNA-directed RNA polymerase complex [GO:0000428]; DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270]; DNA-templated transcription [GO:0006351]
Gene Ontology (molecular function) DNA binding [GO:0003677]; DNA-directed RNA polymerase activity [GO:0003899]; magnesium ion binding [GO:0000287]; zinc ion binding [GO:0008270]
Gene Ontology IDs GO:0000287; GO:0000428; GO:0003677; GO:0003899; GO:0005829; GO:0006351; GO:0008270
Protein families RNA polymerase beta' chain family
Sequence similarities SIMILARITY: Belongs to the RNA polymerase beta' chain family. {ECO:0000255|HAMAP-Rule:MF_01322}.
Annotation Summary

Sequence features and PTMs

Chain CHAIN 1..1316; /note="DNA-directed RNA polymerase subunit beta'"; /id="PRO_0000067760"